NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
DOI=10.1101/gr.1285603; PubMed=12840036 [NCBI, ExPASy, EBI, Israel, Japan]
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens.";
Genome Res. 13:1572-1579(2003).

Comments

FUNCTION: Catalyzes the NAD(+)-dependent oxidation of both quinate and shikimate to 3-dehydroquinate and 3-dehydroshikimate, respectively. Seems to play a key role in the quinate degradation pathway (By similarity).
CATALYTIC ACTIVITY: Quinate + NAD⁺ = 3-dehydroquinate + NADH.
CATALYTIC ACTIVITY: Shikimate + NAD⁺ = 3-dehydroshikimate + NADH.
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 4/7 .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the shikimate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000035; BAC17253.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_737053.1; -.

3D structure databases

HSSP

Q58484; 1NVT. [HSSP ENTRY / PDB]

SMR

Q8FSF0; 4-284.

ModBase

Q8FSF0.

Enzyme and pathway databases

BioCyc

CEFF196164:CE0443-MON; -.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0030266;	Molecular function: quinate 5-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0004764;	Molecular function: shikimate 5-dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0009073;	Biological process: aromatic amino acid family biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00222; atypical; 1.
PBIL [Tree]

InterPro

IPR016040; NAD(P)-bd.
IPR005097; Saccharopine_DHase.
IPR013708; Shikimate_DHase-bd_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF03435; Saccharop_dh; 1.
PF08501; Shikimate_dh_N; 1.
Pfam graphical view of domain structure.

Genome annotation databases

1034899; -.

BA000035_GR; CE0443.

cef:CE0443; -.

fig|196164.1.peg.443; -.

Phylogenomic databases

HOGENOM

Q8FSF0; -.

Genome annotation databases

CMR

Q8FSF0; CE0443.

Other

ProtoNet

Q8FSF0.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 284`	`284`	`Quinate/shikimate dehydrogenase.`	`PRO_0000325114`
`NP_BIND`	`135 139`	`5`	`NAD (By similarity).`
`NP_BIND`	`252 256`	`5`	`NAD (By similarity).`
`ACT_SITE`	`74 74`		`Proton acceptor (Potential).`
`BINDING`	`111 111`		`Substrate (By similarity).`
`BINDING`	`159 159`		`NAD (By similarity).`

Sequence information

Length: 284 AA [This is the length of the unprocessed precursor]

Molecular weight: 29938 Da [This is the MW of the unprocessed precursor]

CRC64: 7179FA02CF0DE537 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNHDSILLGL IGEDISLSRT PAMHEAEGLA QGAATVYRRI DTLTDRARGR SLQELLDAAR 

        70         80         90        100        110        120 
STGFNGLNIT HPYKQAVLPL LDEVSEQAAQ LGAVNTVVIG EDGRTSGHNT DVTGFARGLE 

       130        140        150        160        170        180 
EGLPDATMTT VVQVGAGGVG NAVAYSLVTH GVEQLQVADL DPARAQALAD AINSAIGREA 

       190        200        210        220        230        240 
VHGIDARGVE EAIAAADGVV NATPMGMLAH PGTAFDTSCL TPHHWVGDVV YMPIETQLLK 

       250        260        270        280 
DARALGCRTL DGTRMAIHQA VDAFRLFTGL EPDVERMRAT FLSL

Q8FSF0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools